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Database: UniProt
Entry: C1DIJ2_AZOVD
LinkDB: C1DIJ2_AZOVD
Original site: C1DIJ2_AZOVD 
ID   C1DIJ2_AZOVD            Unreviewed;       691 AA.
AC   C1DIJ2;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=4-alpha-glucanotransferase {ECO:0000256|ARBA:ARBA00020295, ECO:0000256|RuleBase:RU361207};
DE            EC=2.4.1.25 {ECO:0000256|ARBA:ARBA00012560, ECO:0000256|RuleBase:RU361207};
DE   AltName: Full=Amylomaltase {ECO:0000256|ARBA:ARBA00031423, ECO:0000256|RuleBase:RU361207};
DE   AltName: Full=Disproportionating enzyme {ECO:0000256|ARBA:ARBA00031501, ECO:0000256|RuleBase:RU361207};
GN   Name=malQ {ECO:0000313|EMBL:ACO78673.1};
GN   OrderedLocusNames=Avin_24890 {ECO:0000313|EMBL:ACO78673.1};
OS   Azotobacter vinelandii (strain DJ / ATCC BAA-1303).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=322710 {ECO:0000313|EMBL:ACO78673.1, ECO:0000313|Proteomes:UP000002424};
RN   [1] {ECO:0000313|EMBL:ACO78673.1, ECO:0000313|Proteomes:UP000002424}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DJ / ATCC BAA-1303 {ECO:0000313|Proteomes:UP000002424};
RX   PubMed=19429624; DOI=10.1128/JB.00504-09;
RA   Setubal J.C., dos Santos P., Goldman B.S., Ertesvag H., Espin G.,
RA   Rubio L.M., Valla S., Almeida N.F., Balasubramanian D., Cromes L.,
RA   Curatti L., Du Z., Godsy E., Goodner B., Hellner-Burris K., Hernandez J.A.,
RA   Houmiel K., Imperial J., Kennedy C., Larson T.J., Latreille P., Ligon L.S.,
RA   Lu J., Maerk M., Miller N.M., Norton S., O'Carroll I.P., Paulsen I.,
RA   Raulfs E.C., Roemer R., Rosser J., Segura D., Slater S., Stricklin S.L.,
RA   Studholme D.J., Sun J., Viana C.J., Wallin E., Wang B., Wheeler C., Zhu H.,
RA   Dean D.R., Dixon R., Wood D.;
RT   "Genome sequence of Azotobacter vinelandii, an obligate aerobe specialized
RT   to support diverse anaerobic metabolic processes.";
RL   J. Bacteriol. 191:4534-4545(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Transfers a segment of a (1->4)-alpha-D-glucan to a new
CC         position in an acceptor, which may be glucose or a (1->4)-alpha-D-
CC         glucan.; EC=2.4.1.25; Evidence={ECO:0000256|ARBA:ARBA00000439,
CC         ECO:0000256|RuleBase:RU361207};
CC   -!- SIMILARITY: Belongs to the disproportionating enzyme family.
CC       {ECO:0000256|ARBA:ARBA00005684, ECO:0000256|RuleBase:RU361207}.
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DR   EMBL; CP001157; ACO78673.1; -; Genomic_DNA.
DR   RefSeq; WP_012701066.1; NC_012560.1.
DR   AlphaFoldDB; C1DIJ2; -.
DR   STRING; 322710.Avin_24890; -.
DR   CAZy; GH77; Glycoside Hydrolase Family 77.
DR   EnsemblBacteria; ACO78673; ACO78673; Avin_24890.
DR   KEGG; avn:Avin_24890; -.
DR   eggNOG; COG1640; Bacteria.
DR   HOGENOM; CLU_022072_1_0_6; -.
DR   OrthoDB; 9763489at2; -.
DR   Proteomes; UP000002424; Chromosome.
DR   GO; GO:0004134; F:4-alpha-glucanotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102500; F:beta-maltose 4-alpha-glucanotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR003385; Glyco_hydro_77.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   NCBIfam; TIGR00217; malQ; 1.
DR   PANTHER; PTHR32438; 4-ALPHA-GLUCANOTRANSFERASE DPE1, CHLOROPLASTIC/AMYLOPLASTIC; 1.
DR   PANTHER; PTHR32438:SF5; 4-ALPHA-GLUCANOTRANSFERASE DPE1, CHLOROPLASTIC_AMYLOPLASTIC; 1.
DR   Pfam; PF02446; Glyco_hydro_77; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361207};
KW   Glycosyltransferase {ECO:0000256|RuleBase:RU361207};
KW   Transferase {ECO:0000256|RuleBase:RU361207, ECO:0000313|EMBL:ACO78673.1}.
SQ   SEQUENCE   691 AA;  76059 MW;  469491A42F5FD2A2 CRC64;
     MSNDERLRTL AAAAGIAVDW IDAEGRPRKV TPEVLRRVLA ELELPADSGG QIADSLEQLR
     RMSGELPPLL TLERGQSLDL SGHFEPGSTF ELTLEDGRRH SGRLDEQARL PPIEQPGYHR
     LAIGAQSLTL AVAPPRCIGL DALSGHPSPR LWGLAVQLYS LRRQGDGGIG DTQALENLVH
     RAAREGAAGI AISPLHAMFS ADTQRFSPYS PSSRLFYNVL HSAPGSILGE REVRTALEAG
     GLADEWQRLE RLELIDWPAA ADAKLRLLRL LHAEFRQGGN PLEQDFASFR RNGGEALDNH
     CRFEALHAYH VRHHGLYDWR RWDPALRCPG SAAVAGFARE YEDEITFHAF AQWLIVRGLE
     RTQHAARSAG MPIGLIADLA VGADGGGSQA WSRQAELLPS LTVGAPPDIL NRSGQSWGVS
     AFSPWGLRQH GFHAFIEMLR ANLAHAGGIR IDHVMGLRRL WLIPPGAEQR DGAYLHYPQE
     DLMRLLALES WRHGAAILGE DLGTVPEGFR PLLAERGILG MRVLLFEQDD DGRFARPRQW
     PGDALATSTT HDLPTLAGWW RERDIDWRER LRLADAEASE AARRTRRRER LALREALADS
     GGPALDEPLD SDGLIDACVR FLGATPAPLV LLPMEDALGL DEQANLPGTI DGHPNWRRRL
     PVESDGLLDD AAPARRLCLL KEARGTPGGR S
//
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